Our hosting provider is investigating network issues. We apologize for the inconvenience.

Searching across hundreds of databases

Our searching services are busy right now. Your search will reload in five seconds.

X
Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

Role of ANC-1 in tethering nuclei to the actin cytoskeleton.

Science (New York, N.Y.) | Oct 11, 2002

Mutations in anc-1 (nuclear anchorage defective) disrupt the positioning of nuclei and mitochondria in Caenorhabditis elegans. ANC-1 is shown to consist of mostly coiled regions with a nuclear envelope localization domain (called the KASH domain) and an actin-binding domain; this structure was conserved with the Drosophila protein Msp-300 and the mammalian Syne proteins. Antibodies against ANC-1 localized cytoplasmically and were enriched at the nuclear periphery in an UNC-84-dependent manner. Overexpression of the KASH domain or the actin-binding domain caused a dominant negative anchorage defect. Thus, ANC-1 may connect nuclei to the cytoskeleton by interacting with UNC-84 at the nuclear envelope and with actin in the cytoplasm.

Pubmed ID: 12169658 RIS Download

Mesh terms: Actins | Alleles | Animals | Animals, Genetically Modified | Caenorhabditis elegans | Caenorhabditis elegans Proteins | Cell Nucleus | Cytoplasm | Cytoskeleton | Genes, Helminth | Membrane Glycoproteins | Microfilament Proteins | Mitochondria | Mutation | Nuclear Envelope | Nuclear Proteins | Phenotype | Protein Binding | Protein Structure, Tertiary | Recombinant Fusion Proteins

Publication data is provided by the National Library of Medicine ® and PubMed ®. Data is retrieved from PubMed ® on a weekly schedule. For terms and conditions see the National Library of Medicine Terms and Conditions.

We have not found any resources mentioned in this publication.